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7AM7

Crystal structure of Peptiligase mutant - M222P/L217H/A225N/F189W/N218D

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
A0008236molecular_functionserine-type peptidase activity
B0004252molecular_functionserine-type endopeptidase activity
B0006508biological_processproteolysis
B0008236molecular_functionserine-type peptidase activity
C0004252molecular_functionserine-type endopeptidase activity
C0006508biological_processproteolysis
C0008236molecular_functionserine-type peptidase activity
Functional Information from PROSITE/UniProt
site_idPS00136
Number of Residues12
DetailsSUBTILASE_ASP Serine proteases, subtilase family, aspartic acid active site. VAVIDSGIdssH
ChainResidueDetails
AVAL28-HIS39
BVAL28-HIS39

site_idPS00137
Number of Residues11
DetailsSUBTILASE_HIS Serine proteases, subtilase family, histidine active site. HGThVAGtVLA
ChainResidueDetails
BHIS64-ALA74
AHIS64-ALA74

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsSITE: Reactive bond
ChainResidueDetails
CASP32
CHIS64
CALA230
PLEU77
BHIS64
BALA230

site_idSWS_FT_FI2
Number of Residues9
DetailsBINDING:
ChainResidueDetails
BGLY178
BVAL180
BSER183
CLYS2
CASP41
CVAL75
CPRO86
CALA88
CLEU90
CGLY178
CVAL180
CSER183
BPRO86
BALA88
BLEU90
BLYS2
BASP41
BVAL75

Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 723
ChainResidueDetails
BASP32electrostatic interaction, electrostatic stabiliser
BHIS64proton acceptor, proton donor
BTHR164electrostatic interaction, electrostatic stabiliser
BALA230nucleofuge, nucleophile, proton acceptor, proton donor

site_idMCSA2
Number of Residues4
DetailsM-CSA 723
ChainResidueDetails
CASP32electrostatic interaction, electrostatic stabiliser
CHIS64proton acceptor, proton donor
CTHR164electrostatic interaction, electrostatic stabiliser
CALA230nucleofuge, nucleophile, proton acceptor, proton donor

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PDB entries from 2024-05-15

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